ArticleToxins2016
Isolation of Anti-Ricin Protective Antibodies Exhibiting High Affinity from Immunized Non-Human Primates.
Article in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 46 citations in OpenAlex.
- Rapid and Highly Sensitive Detection of Ricin in Biological Fluids Using Optical Modulation Biosensing.Biosensors · 2025Article
- Article
- Generation of recombinant mAbs to vaccinia virus displaying high affinity and potent neutralization.Microbiology spectrum · 2023Article
- Highly Specific Monoclonal Antibody Targeting the Botulinum Neurotoxin Type E Exposed SNAP-25 Neoepitope.Antibodies (Basel, Switzerland) · 2022Article
- Centaur antibodies: Engineered chimeric equine-human recombinant antibodies.Frontiers in immunology · 2022Article
- The neutralization potency of anti-SARS-CoV-2 therapeutic human monoclonal antibodies is retained against viral variants.Cell reports · 2021Article
- Therapeutic antibodies, targeting the SARS-CoV-2 spike N-terminal domain, protect lethally infected K18-hACE2 mice.iScience · 2021Article
- Epitope Binning of Novel Monoclonal Anti F1 and Anti LcrV Antibodies and Their Application in a Simple, Short, HTRF Test for Clinical Plague Detection.Pathogens (Basel, Switzerland) · 2021Article
- Ricin Antibodies' Neutralizing Capacity against Different Ricin Isoforms and Cultivars.Toxins · 2021Article
- Mapping Immunodominant Antibody Epitopes of Abrin.Antibodies (Basel, Switzerland) · 2020Article
- Article
- Sites of vulnerability on ricin B chain revealed through epitope mapping of toxin-neutralizing monoclonal antibodies.PloS one · 2020Article
- Inhibition of Francisella tularensis phagocytosis using a novel anti-LPS scFv antibody fragment.Scientific reports · 2019Article
- Ricin: An Ancient Story for a Timeless Plant Toxin.Toxins · 2019Review
- Cognizance of Molecular Methods for the Generation of Mutagenic Phage Display Antibody Libraries for Affinity Maturation.International journal of molecular sciences · 2019Review
- Whole-Cell Multiparameter Assay for Ricin and Abrin Activity-Based Digital Holographic Microscopy.Toxins · 2019Article
- A Collection of Single-Domain Antibodies that Crowd Ricin Toxin's Active Site.Antibodies (Basel, Switzerland) · 2018Article
- Article
- Fine-Specificity Epitope Analysis Identifies Contact Points on Ricin Toxin Recognized by Protective Monoclonal Antibodies.ImmunoHorizons · 2018Article
- Contribution of an unusual CDR2 element of a single domain antibody in ricin toxin binding affinity and neutralizing activity.Protein engineering, design & selection : PEDS · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ricin, derived from the castor bean plant Ricinus communis, is one of the most potent and lethal toxins known, against which there is no available antidote. To date, the use of neutralizing antibodies is the most promising post-exposure treatment for ricin intoxication. The aim of this study was to isolate high affinity anti-ricin antibodies that possess potent toxin-neutralization capabilities. Two non-human primates were immunized with either a ricin-holotoxin- or subunit-based vaccine, to ensure the elicitation of diverse high affinity antibodies. By using a comprehensive set of primers, immune scFv phage-displayed libraries were constructed and panned. A panel of 10 antibodies (five directed against the A subunit of ricin and five against the B subunit) was isolated and reformatted into a full-length chimeric IgG. All of these antibodies were found to neutralize ricin in vitro, and several conferred full protection to ricin-intoxicated mice when given six hours after exposure. Six antibodies were found to possess exceptionally high affinity toward the toxin, with KD values below pM (k(off )< 1 × 10(-7) s(-1)) that were well correlated with their ability to neutralize ricin. These antibodies, alone or in combination, could be used for the development of a highly-effective therapeutic preparation for post-exposure treatment of ricin intoxication.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.